2ly8

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[[Image:2ly8.png|left|200px]]
 
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{{STRUCTURE_2ly8| PDB=2ly8 | SCENE= }}
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==The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the centromere-specific Cse4/H4 histone variant==
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<StructureSection load='2ly8' size='340' side='right'caption='[[2ly8]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ly8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LY8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ly8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ly8 OCA], [https://pdbe.org/2ly8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ly8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ly8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ly8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CENPA_YEAST CENPA_YEAST] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Required for functional chromatin architecture at the yeast 2-micron circle partitioning locus and promotes equal plasmid segregation.<ref>PMID:7698647</ref> <ref>PMID:9741625</ref> <ref>PMID:9584087</ref> <ref>PMID:10454560</ref> <ref>PMID:11063678</ref> <ref>PMID:10891506</ref> <ref>PMID:10499801</ref> <ref>PMID:11606525</ref> <ref>PMID:15590827</ref> <ref>PMID:16207811</ref> <ref>PMID:16966420</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In eukaryotes, a variant of conventional histone H3 termed CenH3 epigenetically marks the centromere. The conserved CenH3 chaperone specifically recognizes CenH3 and is required for CenH3 deposition at the centromere. Recently, the structures of the chaperone/CenH3/H4 complexes have been determined for Homo sapiens (Hs) and the budding yeasts Saccharomyces cerevisiae (Sc) and Kluyveromyces lactis (Kl). Surprisingly, the three structures are very different, leading to different proposed structural bases for chaperone function. The question of which structural region of CenH3 provides the specificity determinant for the chaperone recognition is not fully answered. Here, we investigated these issues using solution NMR and site-directed mutagenesis. We discovered that, in contrast to previous findings, the structures of the Kl and Sc chaperone/CenH3/H4 complexes are actually very similar. This new finding reveals that both budding yeast and human chaperones use a similar structural region to block DNA from binding to the histones. Our mutational analyses further indicate that the N-terminal region of the CenH3alpha2 helix is sufficient for specific recognition by the chaperone for both budding yeast and human. Thus, our studies have identified conserved structural bases of how the chaperones recognize CenH3 and perform the chaperone function.
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===The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the centromere-specific Cse4/H4 histone variant===
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Identification of Functionally Conserved Regions in the Structure of the Chaperone/Cen H3/H4 Complex.,Hong J, Feng H, Zhou Z, Ghirlando R, Bai Y J Mol Biol. 2012 Nov 23. pii: S0022-2836(12)00893-5. doi:, 10.1016/j.jmb.2012.11.021. PMID:23178171<ref>PMID:23178171</ref>
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{{ABSTRACT_PUBMED_23178171}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2ly8" style="background-color:#fffaf0;"></div>
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[[2ly8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LY8 OCA].
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Bai, Y.]]
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[[Category: Bai Y]]
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[[Category: Feng, H.]]
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[[Category: Feng H]]
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[[Category: Ghirlando, R.]]
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[[Category: Ghirlando R]]
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[[Category: Hong, J.]]
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[[Category: Hong J]]
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[[Category: Zhou, Z.]]
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[[Category: Zhou Z]]
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[[Category: Cenh3 variant]]
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[[Category: Centromere protein]]
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[[Category: Chaperone]]
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[[Category: Partially unfolded]]
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Current revision

The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the centromere-specific Cse4/H4 histone variant

PDB ID 2ly8

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